Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins
Azadeh Eskandari
1, 2
,
Thean Chor Leow
1, 3, 4
,
Mohd Basyaruddin Abdul Rahman
5
,
Siti Nurbaya Oslan
1, 2, 4
Publication type: Journal Article
Publication date: 2024-04-11
SJR: —
CiteScore: —
Impact factor: —
ISSN: 09758151, 25244663
General Medicine
Abstract
Protein, being a fundamental biological macromolecule, assumes a critical function in various vital activities of cellular growth, heredity, reproduction, and other biological processes. Moreover, the utilization of recombinant proteins is extensive in the advancement of pharmaceutical materials, enzyme industrial implementation, and fundamental proteomics investigation. Effective purification methods are necessary for the production of recombinant proteins as well as natural proteins and peptides to ensure their efficient production. Various methods have been developed to improve protein purification, incorporating the recent advancements in protein separation technology. This review is focused on the sophisticated approach to the purification techniques of protein, peptide, and recombinant protein. The system known as the multi-column plate adapter (MCPA) proves to be highly cost-effective in the field of protein purification methods. The assessment has determined that the method of employing an aqueous two-phase system (ATPS) is an economically sound, and highly efficient approach in protein purification. Thus, the ATPS might represent a feasible approach to single-stage purification, deviating from the complex chromatography procedure. The chromatography strategies have been improved for the purification of peptides including batch liquid, continuous and semi-continuous chromatography. In the realm of recombinant protein purification, affinity purification presents several advantages compared to alternative methods. To produce, identify, and purify recombinant proteins from their host systems in large quantities with high efficiency, affinity strategies—particularly fusion strategies—have been developed. Hence, the purpose of this review is to implement the various purification technologies, their potential employments, fundamentals, advantages, and limitations.
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5
Total citations:
5
Citations from 2024:
5
(100%)
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MLA
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GOST
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Eskandari A. et al. Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins // Journal of Proteins and Proteomics. 2024. Vol. 15. No. 2. pp. 233-257.
GOST all authors (up to 50)
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Eskandari A., Leow T. C., Rahman M. B. A., Oslan S. N. Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins // Journal of Proteins and Proteomics. 2024. Vol. 15. No. 2. pp. 233-257.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1007/s42485-024-00139-7
UR - https://link.springer.com/10.1007/s42485-024-00139-7
TI - Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins
T2 - Journal of Proteins and Proteomics
AU - Eskandari, Azadeh
AU - Leow, Thean Chor
AU - Rahman, Mohd Basyaruddin Abdul
AU - Oslan, Siti Nurbaya
PY - 2024
DA - 2024/04/11
PB - Springer Nature
SP - 233-257
IS - 2
VL - 15
SN - 0975-8151
SN - 2524-4663
ER -
Cite this
BibTex (up to 50 authors)
Copy
@article{2024_Eskandari,
author = {Azadeh Eskandari and Thean Chor Leow and Mohd Basyaruddin Abdul Rahman and Siti Nurbaya Oslan},
title = {Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins},
journal = {Journal of Proteins and Proteomics},
year = {2024},
volume = {15},
publisher = {Springer Nature},
month = {apr},
url = {https://link.springer.com/10.1007/s42485-024-00139-7},
number = {2},
pages = {233--257},
doi = {10.1007/s42485-024-00139-7}
}
Cite this
MLA
Copy
Eskandari, Azadeh, et al. “Utilization and prospect of purification technologies in natural proteins, peptides and recombinant proteins.” Journal of Proteins and Proteomics, vol. 15, no. 2, Apr. 2024, pp. 233-257. https://link.springer.com/10.1007/s42485-024-00139-7.